Hsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes Treatment-Reference-Cited by-同舟云学术

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Hsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes Treatment

Published:2016-03-09 Issue:3 Volume:11 Page:e0149409
ISSN:1932-6203
Container-title:PLOS ONE
language:en
Short-container-title:PLoS ONE

Author:

Rosas Paola C.,Nagaraja Ganachari M.,Kaur Punit,Panossian Alexander,Wickman Georg,Garcia L. Rene,Al-Khamis Fahd A.,Asea Alexzander A. A.

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference41 articles.

1. Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes;RL Hull;J Clin Endocrinol Metab,2004

2. Fate of the beta-cell in the pathophysiology of type 2 diabetes;RK Campbell;Journal of the American Pharmacists Association: JAPhA,2009

3. Islet amyloid polypeptide, islet amyloid, and diabetes mellitus;P Westermark;Physiol Rev,2011

4. Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets;JF Paulsson;Diabetologia,2006

5. Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation;JF Paulsson;Diabetes,2005

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